ID V9GX11_MOUSE Unreviewed; 192 AA. AC V9GX11; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 03-AUG-2022, entry version 53. DE RecName: Full=Transmembrane ascorbate-dependent reductase CYB561 {ECO:0000256|ARBA:ARBA00024231}; DE AltName: Full=Cytochrome b-561 {ECO:0000256|ARBA:ARBA00030896}; DE AltName: Full=Cytochrome b561 {ECO:0000256|ARBA:ARBA00032709}; GN Name=Cyb561 {ECO:0000313|Ensembl:ENSMUSP00000138931, GN ECO:0000313|MGI:MGI:103253}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000138931, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000138931, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000138931, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] {ECO:0000313|Ensembl:ENSMUSP00000138931} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000138931}; RG Ensembl; RL Submitted (DEC-2013) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-ascorbate(in) + monodehydro-L-ascorbate radical(out) = L- CC ascorbate(out) + monodehydro-L-ascorbate radical(in); CC Xref=Rhea:RHEA:66524, ChEBI:CHEBI:38290, ChEBI:CHEBI:59513; CC Evidence={ECO:0000256|ARBA:ARBA00024163}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66525; CC Evidence={ECO:0000256|ARBA:ARBA00024163}; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Evidence={ECO:0000256|ARBA:ARBA00001970}; CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, CC chromaffin granule membrane {ECO:0000256|ARBA:ARBA00024185}; Multi-pass CC membrane protein {ECO:0000256|ARBA:ARBA00024185}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR RefSeq; XP_006532197.1; XM_006532134.3. DR SMR; V9GX11; -. DR Antibodypedia; 18653; 87 antibodies from 17 providers. DR DNASU; 13056; -. DR Ensembl; ENSMUST00000184086.8; ENSMUSP00000138931.2; ENSMUSG00000019590.17. DR GeneID; 13056; -. DR CTD; 1534; -. DR MGI; MGI:103253; Cyb561. DR VEuPathDB; HostDB:ENSMUSG00000019590; -. DR GeneTree; ENSGT00950000183197; -. DR HOGENOM; CLU_069712_3_1_1; -. DR BioGRID-ORCS; 13056; 0 hits in 74 CRISPR screens. DR ChiTaRS; Cyb561; mouse. DR Proteomes; UP000000589; Chromosome 11. DR Bgee; ENSMUSG00000019590; Expressed in choroid plexus of fourth ventricle and 237 other tissues. DR ExpressionAtlas; V9GX11; baseline and differential. DR GO; GO:0042584; C:chromaffin granule membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR InterPro; IPR028837; CYB561. DR InterPro; IPR043205; CYB561/CYBRD1-like. DR InterPro; IPR006593; Cyt_b561/ferric_Rdtase_TM. DR PANTHER; PTHR10106; PTHR10106; 1. DR PANTHER; PTHR10106:SF14; PTHR10106:SF14; 1. DR Pfam; PF03188; Cytochrom_B561; 1. DR SMART; SM00665; B561; 1. DR PROSITE; PS50939; CYTOCHROME_B561; 1. PE 4: Predicted; KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329}; KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00022617}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}. FT TRANSMEM 12..36 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 56..74 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 86..105 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 117..133 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 18..192 FT /note="Cytochrome b561" FT /evidence="ECO:0000259|PROSITE:PS50939" SQ SEQUENCE 192 AA; 21009 MW; 497A84EB2A42CBE7 CRC64; MEHSSASVPA ALPYYVAFSQ LLGLTVVAVT GAWLGLYRGG IAWESSLQFN VHPLCMVIGM IFLQGDALLV YRVFRREAKR TTKILHGLLH VFAFIIALVG LVAVFDYHKK KGYADLYSLH SWCGILVFVL YFVQVPASSW LSRALSPFSG SWVSASSCSL ELHSLCGAAT ALSTFSLVPP SSSSLWAQPY WA //